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Hydrophobic Effect

The tendency of nonpolar molecules to aggregate in aqueous solutions, driving the formation of hydrophobic cores in proteins.
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The statement of the theorem

Consider the free energy change ΔGhydro\Delta G_{hydro} associated with the folding of a protein from an unfolded state (U) to a folded state (N) in an aqueous solvent. This effect is primarily driven by the increase in solvent entropy SsolventS_{solvent} upon burial of nonpolar surface area AnonpolarA_{nonpolar}: ΔGhydro=−TΔSsolvent=TΔSsolvent≈γAnonpolar,\Delta G_{hydro} = -T \Delta S_{solvent} = T \Delta S_{solvent} \approx \gamma A_{nonpolar}, where γ\gamma is the surface tension coefficient related to the nonpolar solute-water interaction, and AnonpolarA_{nonpolar} is the total nonpolar surface area buried in the core of the native state relative to the unfolded state.